Identification of domains on the extrinsic 33-kDa protein possibly involved in electrostatic interaction with photosystem II complex by means of chemical modification

Taro Miura, Jian-Ren Shen, Seitaro Takahashi, Masaharu Kamo, Eriko Nakamura, Hisataka Ohta, Ayako Kamei, Yasunori Inoue, Naoshi Domae, Koji Takio, Katsuyoshi Nakazato, Yorinao Inoue, Isao Enami

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

The extrinsic 33-kDa protein of photosystem II (PSII) was modified with various reagents, and the resulting proteins were checked for the ability to rebind to PSII and to reactivate oxygen evolution. While modification of more than eight carboxyl groups of aspartyl and glutamyl residues with glycine methyl ester did not affect the rebinding and reactivating capabilities, modification of amino groups of lysyl residues with either N-succinimidyl propionate or 2,4,6-trinitrobenzene sulfonic acid or modification of guanidino groups of arginyl residues with 2,3-butanedione resulted in a loss of rebinding and reactivating capabilities of the 33-kDa protein. Moreover, the number of lysyl and arginyl residues susceptible to modification was significantly decreased when the protein was bound to PSII as compared with when it was free in solution, whereas the number of carboxyl groups modified was little affected. These results suggested that positive charges are important for the electrostatic interaction between the extrinsic 33-kDa protein and PSII intrinsic proteins, whereas negative charges on the protein do not contribute to such interaction. By a combination of protease digestion and mass spectroscopic analysis, the domains of lysyl residues accessible to N-succinimidyl propionate or 2,4,6-trinitrobenzene sulfonic acid modification only when the 33-kDa protein is free in solution were determined to be Lys 4, Lys 20, Lys 66-Lys 76, Lys 101, Lys 105, Lys 130, Lys 159, Lys 186, and Lys 230-Lys 236. These domains include those previously reported accessible to N-hydroxysuccinimidoblotin only in solution (Frankel and Bricker (1995) Biochemistry 34, 7492-7497), and may be important for the interaction of the 33-kDa protein with PSII intrinsic proteins.

Original languageEnglish
Pages (from-to)3788-3798
Number of pages11
JournalJournal of Biological Chemistry
Volume272
Issue number6
DOIs
Publication statusPublished - 1997
Externally publishedYes

Fingerprint

Photosystem II Protein Complex
Chemical modification
Coulomb interactions
Static Electricity
Proteins
Sulfonic Acids
Diacetyl
Biochemistry
Spectroscopic analysis
Digestion
Peptide Hydrolases
Oxygen

ASJC Scopus subject areas

  • Biochemistry

Cite this

Identification of domains on the extrinsic 33-kDa protein possibly involved in electrostatic interaction with photosystem II complex by means of chemical modification. / Miura, Taro; Shen, Jian-Ren; Takahashi, Seitaro; Kamo, Masaharu; Nakamura, Eriko; Ohta, Hisataka; Kamei, Ayako; Inoue, Yasunori; Domae, Naoshi; Takio, Koji; Nakazato, Katsuyoshi; Inoue, Yorinao; Enami, Isao.

In: Journal of Biological Chemistry, Vol. 272, No. 6, 1997, p. 3788-3798.

Research output: Contribution to journalArticle

Miura, T, Shen, J-R, Takahashi, S, Kamo, M, Nakamura, E, Ohta, H, Kamei, A, Inoue, Y, Domae, N, Takio, K, Nakazato, K, Inoue, Y & Enami, I 1997, 'Identification of domains on the extrinsic 33-kDa protein possibly involved in electrostatic interaction with photosystem II complex by means of chemical modification', Journal of Biological Chemistry, vol. 272, no. 6, pp. 3788-3798. https://doi.org/10.1074/jbc.272.6.3788
Miura, Taro ; Shen, Jian-Ren ; Takahashi, Seitaro ; Kamo, Masaharu ; Nakamura, Eriko ; Ohta, Hisataka ; Kamei, Ayako ; Inoue, Yasunori ; Domae, Naoshi ; Takio, Koji ; Nakazato, Katsuyoshi ; Inoue, Yorinao ; Enami, Isao. / Identification of domains on the extrinsic 33-kDa protein possibly involved in electrostatic interaction with photosystem II complex by means of chemical modification. In: Journal of Biological Chemistry. 1997 ; Vol. 272, No. 6. pp. 3788-3798.
@article{74bbc3e40f9743d389185d47828f6551,
title = "Identification of domains on the extrinsic 33-kDa protein possibly involved in electrostatic interaction with photosystem II complex by means of chemical modification",
abstract = "The extrinsic 33-kDa protein of photosystem II (PSII) was modified with various reagents, and the resulting proteins were checked for the ability to rebind to PSII and to reactivate oxygen evolution. While modification of more than eight carboxyl groups of aspartyl and glutamyl residues with glycine methyl ester did not affect the rebinding and reactivating capabilities, modification of amino groups of lysyl residues with either N-succinimidyl propionate or 2,4,6-trinitrobenzene sulfonic acid or modification of guanidino groups of arginyl residues with 2,3-butanedione resulted in a loss of rebinding and reactivating capabilities of the 33-kDa protein. Moreover, the number of lysyl and arginyl residues susceptible to modification was significantly decreased when the protein was bound to PSII as compared with when it was free in solution, whereas the number of carboxyl groups modified was little affected. These results suggested that positive charges are important for the electrostatic interaction between the extrinsic 33-kDa protein and PSII intrinsic proteins, whereas negative charges on the protein do not contribute to such interaction. By a combination of protease digestion and mass spectroscopic analysis, the domains of lysyl residues accessible to N-succinimidyl propionate or 2,4,6-trinitrobenzene sulfonic acid modification only when the 33-kDa protein is free in solution were determined to be Lys 4, Lys 20, Lys 66-Lys 76, Lys 101, Lys 105, Lys 130, Lys 159, Lys 186, and Lys 230-Lys 236. These domains include those previously reported accessible to N-hydroxysuccinimidoblotin only in solution (Frankel and Bricker (1995) Biochemistry 34, 7492-7497), and may be important for the interaction of the 33-kDa protein with PSII intrinsic proteins.",
author = "Taro Miura and Jian-Ren Shen and Seitaro Takahashi and Masaharu Kamo and Eriko Nakamura and Hisataka Ohta and Ayako Kamei and Yasunori Inoue and Naoshi Domae and Koji Takio and Katsuyoshi Nakazato and Yorinao Inoue and Isao Enami",
year = "1997",
doi = "10.1074/jbc.272.6.3788",
language = "English",
volume = "272",
pages = "3788--3798",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "6",

}

TY - JOUR

T1 - Identification of domains on the extrinsic 33-kDa protein possibly involved in electrostatic interaction with photosystem II complex by means of chemical modification

AU - Miura, Taro

AU - Shen, Jian-Ren

AU - Takahashi, Seitaro

AU - Kamo, Masaharu

AU - Nakamura, Eriko

AU - Ohta, Hisataka

AU - Kamei, Ayako

AU - Inoue, Yasunori

AU - Domae, Naoshi

AU - Takio, Koji

AU - Nakazato, Katsuyoshi

AU - Inoue, Yorinao

AU - Enami, Isao

PY - 1997

Y1 - 1997

N2 - The extrinsic 33-kDa protein of photosystem II (PSII) was modified with various reagents, and the resulting proteins were checked for the ability to rebind to PSII and to reactivate oxygen evolution. While modification of more than eight carboxyl groups of aspartyl and glutamyl residues with glycine methyl ester did not affect the rebinding and reactivating capabilities, modification of amino groups of lysyl residues with either N-succinimidyl propionate or 2,4,6-trinitrobenzene sulfonic acid or modification of guanidino groups of arginyl residues with 2,3-butanedione resulted in a loss of rebinding and reactivating capabilities of the 33-kDa protein. Moreover, the number of lysyl and arginyl residues susceptible to modification was significantly decreased when the protein was bound to PSII as compared with when it was free in solution, whereas the number of carboxyl groups modified was little affected. These results suggested that positive charges are important for the electrostatic interaction between the extrinsic 33-kDa protein and PSII intrinsic proteins, whereas negative charges on the protein do not contribute to such interaction. By a combination of protease digestion and mass spectroscopic analysis, the domains of lysyl residues accessible to N-succinimidyl propionate or 2,4,6-trinitrobenzene sulfonic acid modification only when the 33-kDa protein is free in solution were determined to be Lys 4, Lys 20, Lys 66-Lys 76, Lys 101, Lys 105, Lys 130, Lys 159, Lys 186, and Lys 230-Lys 236. These domains include those previously reported accessible to N-hydroxysuccinimidoblotin only in solution (Frankel and Bricker (1995) Biochemistry 34, 7492-7497), and may be important for the interaction of the 33-kDa protein with PSII intrinsic proteins.

AB - The extrinsic 33-kDa protein of photosystem II (PSII) was modified with various reagents, and the resulting proteins were checked for the ability to rebind to PSII and to reactivate oxygen evolution. While modification of more than eight carboxyl groups of aspartyl and glutamyl residues with glycine methyl ester did not affect the rebinding and reactivating capabilities, modification of amino groups of lysyl residues with either N-succinimidyl propionate or 2,4,6-trinitrobenzene sulfonic acid or modification of guanidino groups of arginyl residues with 2,3-butanedione resulted in a loss of rebinding and reactivating capabilities of the 33-kDa protein. Moreover, the number of lysyl and arginyl residues susceptible to modification was significantly decreased when the protein was bound to PSII as compared with when it was free in solution, whereas the number of carboxyl groups modified was little affected. These results suggested that positive charges are important for the electrostatic interaction between the extrinsic 33-kDa protein and PSII intrinsic proteins, whereas negative charges on the protein do not contribute to such interaction. By a combination of protease digestion and mass spectroscopic analysis, the domains of lysyl residues accessible to N-succinimidyl propionate or 2,4,6-trinitrobenzene sulfonic acid modification only when the 33-kDa protein is free in solution were determined to be Lys 4, Lys 20, Lys 66-Lys 76, Lys 101, Lys 105, Lys 130, Lys 159, Lys 186, and Lys 230-Lys 236. These domains include those previously reported accessible to N-hydroxysuccinimidoblotin only in solution (Frankel and Bricker (1995) Biochemistry 34, 7492-7497), and may be important for the interaction of the 33-kDa protein with PSII intrinsic proteins.

UR - http://www.scopus.com/inward/record.url?scp=15644383206&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=15644383206&partnerID=8YFLogxK

U2 - 10.1074/jbc.272.6.3788

DO - 10.1074/jbc.272.6.3788

M3 - Article

C2 - 9013637

AN - SCOPUS:15644383206

VL - 272

SP - 3788

EP - 3798

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 6

ER -